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Database: UniProt
Entry: B8M9E7_TALSN
LinkDB: B8M9E7_TALSN
Original site: B8M9E7_TALSN 
ID   B8M9E7_TALSN            Unreviewed;      1118 AA.
AC   B8M9E7;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 77.
DE   SubName: Full=SNF2 family helicase/ATPase, putative {ECO:0000313|EMBL:EED17707.1};
GN   ORFNames=TSTA_115070 {ECO:0000313|EMBL:EED17707.1};
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS   1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441959 {ECO:0000313|EMBL:EED17707.1, ECO:0000313|Proteomes:UP000001745};
RN   [1] {ECO:0000313|EMBL:EED17707.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 10500 {ECO:0000313|EMBL:EED17707.1};
RA   Zhao H., Waite J.H.;
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000001745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC   {ECO:0000313|Proteomes:UP000001745};
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC       {ECO:0000256|ARBA:ARBA00009687}.
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DR   EMBL; EQ962655; EED17707.1; -; Genomic_DNA.
DR   EMBL; EQ962655; EED17708.1; -; Genomic_DNA.
DR   RefSeq; XP_002481699.1; XM_002481654.1.
DR   RefSeq; XP_002481700.1; XM_002481655.1.
DR   AlphaFoldDB; B8M9E7; -.
DR   STRING; 441959.B8M9E7; -.
DR   GeneID; 8101317; -.
DR   VEuPathDB; FungiDB:TSTA_115070; -.
DR   eggNOG; KOG0385; Eukaryota.
DR   HOGENOM; CLU_000315_0_2_1; -.
DR   InParanoid; B8M9E7; -.
DR   OMA; VHDYQFF; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000001745; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR   CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR   CDD; cd00167; SANT; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR   Gene3D; 1.20.5.1190; iswi atpase; 1.
DR   Gene3D; 1.10.1040.30; ISWI, HAND domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR044754; Isw1/2_DEXHc.
DR   InterPro; IPR015194; ISWI_HAND-dom.
DR   InterPro; IPR036306; ISWI_HAND-dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR017884; SANT_dom.
DR   InterPro; IPR015195; SLIDE.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR   PANTHER; PTHR45623:SF49; ISW-1; 1.
DR   Pfam; PF09110; HAND; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF09111; SLIDE; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00717; SANT; 2.
DR   SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51293; SANT; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000313|EMBL:EED17707.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001745}.
FT   DOMAIN          198..363
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          494..645
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          863..910
FT                   /note="SANT"
FT                   /evidence="ECO:0000259|PROSITE:PS51293"
FT   REGION          1..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          129..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1036..1118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..74
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1038..1057
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1091..1111
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1118 AA;  128315 MW;  55D1DCDDB3C70E1A CRC64;
     MAPSRNLPDS DTSSQVDTPM TDGNESVARI PVDEPDYPMA DSDTNPNTTA SSIAGDLTHT
     DGRKRRSEAF QLRKSVLGKQ HGRLDESRED DSIRRFRYLL GLTDLFRHFI ETNPNPRIKE
     ILAEIDRQNA DETSKAKGSS RKGGASGDRR RRTEKEEDAE LLKDEKSGGE TATIFRESPA
     FINGEMRDYQ IAGLNWLVSL HENGISGILA DEMGLGKTLQ TISFLGYLRH ICGINGPHLV
     VVPKSTLHNW KMEFAKWTPE VNVMVLQGTK EERHELITER LEKEDFDVCI TSYEMILKEK
     SHFKKLAWEY IIIDEAHRIK NEESSLSQII RVFHSRNRLL ITGTPLQNNL HELWALLNFL
     LPDVFGDSEA FDQWFSNQDS DQDTVVQQLH RVLRPFLLRR VKSDVEKSLL PKKEVNLFVG
     MSDMQVKWYQ KILEKDIDAV NGAAGKRESK TRLLNIVMQL RKCCNHPYLF EGAEPGPPYT
     TDEHLIDNSG KMVVLDKILN RMKKQGSRVL IFSQMSRVLD ILEDYCVFRE HKYCRIDGST
     AHEDRIAAID EYNREGSDKF IFLLTTRAGG LGINLTTADI VVLFDSDWNP QADLQAMDRA
     HRIGQKKQVV VFRFVTEHAI EEKVLERAAQ KLRLDQLVIQ QGRTQQQTKN AASKDELLGM
     IQHGAADVFK KQGGTLTGGA EMTDDDIDAI LRKGEERTAE LNKKYEKLGI DDLQKFTSDN
     AYEWNGEDFT NRKKDIGISW INPAKRERKE QFYSIDKYYR QALATGGRTA DPKPKVPRAP
     KQVSIHDWQF FPPRLHELQE KETAYFHKEI GYKAVLADGT DEDLSEREAN RDLEQQEIDN
     AVPLTEEEQA EKARLSEMGF LHWNRRDFQQ FVNGSAKFGR TDYEGIATEV DSKTPQEVKE
     YAKVFWDRYD EINDYPKYIR VIEQGEEKLR KNTHQRKMLR KKLDMYRVPL QQLKINYTVS
     TTNKKVYSEE EDRFLLVMLD KLGKEDDTEG IQLFERMREE IRESPLFRFD WFFLSRTPVE
     LSRRCTTLLN TIAREFEPEP KANGESGKAR GRDRDRVEED GDEDEDEAPA KKKSKNGAAV
     NKKLKGVKAG SKGSSASTSR AASVSSNVQS SKSKSKKK
//
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